Comparative structural elucidation of the K18, K22, and K100 antigens of Escherichia coli as related ribosyl-ribitol phosphates
| Autor: | Maria-Luisa Rodriguez, Klaus Jann, Barbara Jann |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Magnetic Resonance Spectroscopy
Stereochemistry Enzyme-Linked Immunosorbent Assay medicine.disease_cause Ribitol Methylation Biochemistry Mass Spectrometry Analytical Chemistry chemistry.chemical_compound Antigen Ribose Carbohydrate Conformation Escherichia coli medicine Moiety Immunoelectrophoresis biology Hemagglutination Polysaccharides Bacterial Organic Chemistry General Medicine biology.organism_classification Enterobacteriaceae Carbohydrate Sequence chemistry Acetylation Alkaline phosphatase Indicators and Reagents |
| Zdroj: | Carbohydrate Research. 173:243-253 |
| ISSN: | 0008-6215 |
| Popis: | The structures of the capsular K18, K22, and K100 antigens of E. coli O23:K18:H15, O23:K22:H15, and O75:K100:H5, respectively, were elucidated by determination of composition, 1 H-, 13 C- and 31 P-n.m.r. spectroscopy, periodate oxidation, alkaline hydrolysis followed by incubation with alkaline phosphatase, and methylation analysis of the polymers and their neutral fragmentation products. The polymers are poly(ribosyl-ribitol phosphates) related to the capsular antigen of H. influenzae (H i b). The K22 antigen has the repeating unit -P-2)-β-Rib-(1→2)-RibOH-(5-, and the K18 antigen has the same polymer chain with partial 3- O -acetylation of the ribose moiety. The K100 antigen consists of repeating units of -P-3)-β-Rib-(1→2)-RibOH-(5- and seems to have a secondary structure different from that of the other antigens. Together with the H i b capsular antigens, the structure of which was reported as -P-3)-β-Rib-(1→1)-RibOH-(5-, these capsular antigens represent a structurally related group of capsular polymers. |
| Databáze: | OpenAIRE |
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